Structural Basis for Protein Recognition by B30.2/SPRY Domains

Jae Sung Woo, Hye Young Suh, Sam Yong Park, Byung Ha Oh

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.

Original languageEnglish
Pages (from-to)967-976
Number of pages10
JournalMolecular Cell
Volume24
Issue number6
DOIs
Publication statusPublished - 2006 Dec 28
Externally publishedYes

Fingerprint

Peptides
Proteins
Suppressor of Cytokine Signaling Proteins
RNA Helicases
Binding Sites
Cytokines
Amino Acids
B30.2-SPRY Domain

Keywords

  • SIGNALING

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Structural Basis for Protein Recognition by B30.2/SPRY Domains. / Woo, Jae Sung; Suh, Hye Young; Park, Sam Yong; Oh, Byung Ha.

In: Molecular Cell, Vol. 24, No. 6, 28.12.2006, p. 967-976.

Research output: Contribution to journalArticle

Woo, Jae Sung ; Suh, Hye Young ; Park, Sam Yong ; Oh, Byung Ha. / Structural Basis for Protein Recognition by B30.2/SPRY Domains. In: Molecular Cell. 2006 ; Vol. 24, No. 6. pp. 967-976.
@article{92d4ca7ac39d4986b7d411bb2fd3ce76,
title = "Structural Basis for Protein Recognition by B30.2/SPRY Domains",
abstract = "B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.",
keywords = "SIGNALING",
author = "Woo, {Jae Sung} and Suh, {Hye Young} and Park, {Sam Yong} and Oh, {Byung Ha}",
year = "2006",
month = "12",
day = "28",
doi = "10.1016/j.molcel.2006.11.009",
language = "English",
volume = "24",
pages = "967--976",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "6",

}

TY - JOUR

T1 - Structural Basis for Protein Recognition by B30.2/SPRY Domains

AU - Woo, Jae Sung

AU - Suh, Hye Young

AU - Park, Sam Yong

AU - Oh, Byung Ha

PY - 2006/12/28

Y1 - 2006/12/28

N2 - B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.

AB - B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.

KW - SIGNALING

UR - http://www.scopus.com/inward/record.url?scp=33845663050&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33845663050&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2006.11.009

DO - 10.1016/j.molcel.2006.11.009

M3 - Article

C2 - 17189197

AN - SCOPUS:33845663050

VL - 24

SP - 967

EP - 976

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 6

ER -